NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|19527104|ref|NP_598649|]
View 

acid sphingomyelinase-like phosphodiesterase 3b precursor [Mus musculus]

Protein Classification

acid sphingomyelinase family protein( domain architecture ID 17655516)

acid sphingomyelinase family protein such as human acid sphingomyelinase-like phosphodiesterase 3b, a lipid-modulating phosphodiesterase active on the surface of macrophages and dendritic cells

CATH:  3.60.21.10
EC:  3.1.4.-
Gene Ontology:  GO:0004767|GO:0046872|GO:0006685
PubMed:  15052326|19536191|23579450|8003970|25837850

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 23-323 8.70e-111

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


:

Pssm-ID: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 328.49  E-value: 8.70e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  23 FWHISDLHLDPNYTVSKDPlQVCPSAG--------SQPVLNAGPWGDYLCDSPWALINSSLYAMKEIEPKPDFILWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEY-ANCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  95 TPHVPNESLGEAAVLAIvERLTNLIKEVFPDTKVYAALGNHDFHPKNQFPA---QSNRIYNQVAELWRPWLSNESYALFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPhsnSPSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 172 RGAFYSEKlpgPSRAGRVVVLNTNLYYSNNEQT-AGMADPGEQFRWLGDVLSNASRDGEMVYVIGHVPPGFFEKTQNkaw 250
Cdd:cd00842 159 KGGYYSVD---VKDGLRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD--- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527104 251 fresFNEEYLKVIQKHHRVIAGQFFGHHHTDSFRMFYDNTGA--PINVMFLTPGVTPWKttlpgvvdgANNPGIR 323
Cdd:cd00842 233 ----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTgsPINVAYIAPSVTPYT---------GNNPSFR 294
ASMase_C super family cl44707
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 293-429 5.09e-30

Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges.


The actual alignment was detected with superfamily member pfam19272:

Pssm-ID: 466022  Cd Length: 143  Bit Score: 113.62  E-value: 5.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104   293 PINVMFLTPGVTPWKTTLPGVvdgANNPGIRIFEYDRATLNLKDLVTYFLNLRQANVQETPRWEQEYRLTEAYQVPDASV 372
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104   373 SSMHtALTRIASEPH--ILQRYYVYNSVSYNH-LTCEDSCRIEHVCAIQHVAFNTYATCL 429
Cdd:pfam19272  79 QSLY-GLAKQFAVPHskQFEKYYNYFFVSYDSsIVCEGGCKALQICAIMYLDYSSYTDCI 137
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 23-323 8.70e-111

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 328.49  E-value: 8.70e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  23 FWHISDLHLDPNYTVSKDPlQVCPSAG--------SQPVLNAGPWGDYLCDSPWALINSSLYAMKEIEPKPDFILWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEY-ANCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  95 TPHVPNESLGEAAVLAIvERLTNLIKEVFPDTKVYAALGNHDFHPKNQFPA---QSNRIYNQVAELWRPWLSNESYALFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPhsnSPSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 172 RGAFYSEKlpgPSRAGRVVVLNTNLYYSNNEQT-AGMADPGEQFRWLGDVLSNASRDGEMVYVIGHVPPGFFEKTQNkaw 250
Cdd:cd00842 159 KGGYYSVD---VKDGLRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD--- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527104 251 fresFNEEYLKVIQKHHRVIAGQFFGHHHTDSFRMFYDNTGA--PINVMFLTPGVTPWKttlpgvvdgANNPGIR 323
Cdd:cd00842 233 ----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTgsPINVAYIAPSVTPYT---------GNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 293-429 5.09e-30

Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges.


Pssm-ID: 466022  Cd Length: 143  Bit Score: 113.62  E-value: 5.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104   293 PINVMFLTPGVTPWKTTLPGVvdgANNPGIRIFEYDRATLNLKDLVTYFLNLRQANVQETPRWEQEYRLTEAYQVPDASV 372
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104   373 SSMHtALTRIASEPH--ILQRYYVYNSVSYNH-LTCEDSCRIEHVCAIQHVAFNTYATCL 429
Cdd:pfam19272  79 QSLY-GLAKQFAVPHskQFEKYYNYFFVSYDSsIVCEGGCKALQICAIMYLDYSSYTDCI 137
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
22-332 1.65e-12

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 67.02  E-value: 1.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  22 RFWHISDLHLDPNytvskdplqvcPSAGSQPVLNAgpwgdylcdspwalinsslyAMKEI-EPKPDFILWTGDDTPHVPN 100
Cdd:COG1409   2 RFAHISDLHLGAP-----------DGSDTAEVLAA--------------------ALADInAPRPDFVVVTGDLTDDGEP 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 101 ESLgeAAVLAIVERLtnlikevfpDTKVYAALGNHDFhpknqfpaqSNRIYNQVAELWRPWLSNESYALFKRGAFysekl 180
Cdd:COG1409  51 EEY--AAAREILARL---------GVPVYVVPGNHDI---------RAAMAEAYREYFGDLPPGGLYYSFDYGGV----- 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 181 pgpsragRVVVLNTNLYYSNNeqtaGMADPgEQFRWLGDVLSNASRDgeMVYVIGHVPPGFFEKTQNKAWFRESfnEEYL 260
Cdd:COG1409 106 -------RFIGLDSNVPGRSS----GELGP-EQLAWLEEELAAAPAK--PVIVFLHHPPYSTGSGSDRIGLRNA--EELL 169

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527104 261 KVIQKHHrvIAGQFFGHHHTDSFRMFYdntgapiNVMFLTPGVTPWKTTLPgvvdgannPGIRIFEYDRATL 332
Cdd:COG1409 170 ALLARYG--VDLVLSGHVHRYERTRRD-------GVPYIVAGSTGGQVRLP--------PGYRVIEVDGDGL 224
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 22-159 8.18e-04

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 39.12  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104    22 RFWHISDLHLDPNYTVSKDPLQVCPSagsqpvlnagpwgdylcdspwalinsslyamkeiEPKPDFILWTGDdtphVPNE 101
Cdd:pfam00149   2 RILVIGDLHLPGQLDDLLELLKKLLE----------------------------------EGKPDLVLHAGD----LVDR 43

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19527104   102 SLGEAAVLAIVERLTNLIKevfpdtkVYAALGNHDFHPKNQFPAQSNriYNQVAELWR 159
Cdd:pfam00149  44 GPPSEEVLELLERLIKYVP-------VYLVRGNHDFDYGECLRLYPY--LGLLARPWK 92
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 23-323 8.70e-111

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 328.49  E-value: 8.70e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  23 FWHISDLHLDPNYTVSKDPlQVCPSAG--------SQPVLNAGPWGDYLCDSPWALINSSLYAMKEIEPKPDFILWTGDD 94
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEY-ANCRSPLccrdesgpGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  95 TPHVPNESLGEAAVLAIvERLTNLIKEVFPDTKVYAALGNHDFHPKNQFPA---QSNRIYNQVAELWRPWLSNESYALFK 171
Cdd:cd00842  80 VRHDVDEQTPEETVESE-SNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPhsnSPSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 172 RGAFYSEKlpgPSRAGRVVVLNTNLYYSNNEQT-AGMADPGEQFRWLGDVLSNASRDGEMVYVIGHVPPGFFEKTQNkaw 250
Cdd:cd00842 159 KGGYYSVD---VKDGLRVISLNTNLYYKKNFWLySNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD--- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19527104 251 fresFNEEYLKVIQKHHRVIAGQFFGHHHTDSFRMFYDNTGA--PINVMFLTPGVTPWKttlpgvvdgANNPGIR 323
Cdd:cd00842 233 ----WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKDTgsPINVAYIAPSVTPYT---------GNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 293-429 5.09e-30

Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges.


Pssm-ID: 466022  Cd Length: 143  Bit Score: 113.62  E-value: 5.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104   293 PINVMFLTPGVTPWKTTLPGVvdgANNPGIRIFEYDRATLNLKDLVTYFLNLRQANVQETPRWEQEYRLTEAYQVPDASV 372
Cdd:pfam19272   2 PVNSLFVAPAVTPVKSVLEKE---SNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQP 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104   373 SSMHtALTRIASEPH--ILQRYYVYNSVSYNH-LTCEDSCRIEHVCAIQHVAFNTYATCL 429
Cdd:pfam19272  79 QSLY-GLAKQFAVPHskQFEKYYNYFFVSYDSsIVCEGGCKALQICAIMYLDYSSYTDCI 137
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
22-332 1.65e-12

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 67.02  E-value: 1.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  22 RFWHISDLHLDPNytvskdplqvcPSAGSQPVLNAgpwgdylcdspwalinsslyAMKEI-EPKPDFILWTGDDTPHVPN 100
Cdd:COG1409   2 RFAHISDLHLGAP-----------DGSDTAEVLAA--------------------ALADInAPRPDFVVVTGDLTDDGEP 50

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 101 ESLgeAAVLAIVERLtnlikevfpDTKVYAALGNHDFhpknqfpaqSNRIYNQVAELWRPWLSNESYALFKRGAFysekl 180
Cdd:COG1409  51 EEY--AAAREILARL---------GVPVYVVPGNHDI---------RAAMAEAYREYFGDLPPGGLYYSFDYGGV----- 105

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 181 pgpsragRVVVLNTNLYYSNNeqtaGMADPgEQFRWLGDVLSNASRDgeMVYVIGHVPPGFFEKTQNKAWFRESfnEEYL 260
Cdd:COG1409 106 -------RFIGLDSNVPGRSS----GELGP-EQLAWLEEELAAAPAK--PVIVFLHHPPYSTGSGSDRIGLRNA--EELL 169

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19527104 261 KVIQKHHrvIAGQFFGHHHTDSFRMFYdntgapiNVMFLTPGVTPWKTTLPgvvdgannPGIRIFEYDRATL 332
Cdd:COG1409 170 ALLARYG--VDLVLSGHVHRYERTRRD-------GVPYIVAGSTGGQVRLP--------PGYRVIEVDGDGL 224
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 82-302 8.79e-08

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 53.10  E-value: 8.79e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  82 EPKPDFILWTGDDTPHVPNESLGEAAVLAIVERLTNLikevfpDTKVYAALGNHDFhpknqfpaqsnriYNqvaeLWRPW 161
Cdd:cd07396  44 ESNLAFVVQLGDIIDGYNAKDRSKEALDAVLSILDRL------KGPVHHVLGNHEF-------------YN----FPREY 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 162 LSNESYALFKRGAFYSEKlpgPSRAGRVVVLNTNLYysnneqTAGMADpgEQFRWLGDVLSNASRDGEMVYVIGHVP--P 239
Cdd:cd07396 101 LNHLKTLNGEDAYYYSFS---PGPGFRFLVLDFVKF------NGGIGE--EQLAWLRNELTSADANGEKVIVLSHLPiyP 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19527104 240 GFFEKTQNkAWFResfnEEYLKVIQKHHRVIAgQFFGHHH-----TDSFRMFYDNTGAPINVMFLTPG 302
Cdd:cd07396 170 EAADPQCL-LWNY----EEVLAILESYPCVKA-CFSGHNHeggyeQDSHGVHHVTLEGVLETPPDSQA 231
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 22-159 8.18e-04

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 39.12  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104    22 RFWHISDLHLDPNYTVSKDPLQVCPSagsqpvlnagpwgdylcdspwalinsslyamkeiEPKPDFILWTGDdtphVPNE 101
Cdd:pfam00149   2 RILVIGDLHLPGQLDDLLELLKKLLE----------------------------------EGKPDLVLHAGD----LVDR 43

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19527104   102 SLGEAAVLAIVERLTNLIKevfpdtkVYAALGNHDFHPKNQFPAQSNriYNQVAELWR 159
Cdd:pfam00149  44 GPPSEEVLELLERLIKYVP-------VYLVRGNHDFDYGECLRLYPY--LGLLARPWK 92
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 25-286 1.22e-03

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 40.34  E-value: 1.22e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  25 HISDLHLDPNytvskdplqvcpsagsqpvlnagPWGDYLCDSPWALINSSLYAMKEIEPKPDFILWTGDDTPHvpneslG 104
Cdd:cd07402   3 QISDTHLFAP-----------------------GEGALLGVDTAARLAAAVAQVNALHPRPDLVVVTGDLSDD------G 53

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 105 EAAVLaivERLTNLIKEVfpDTKVYAALGNHDFhpknqfpaqsnriynqVAELWRPWLSNESYALFKRGAFYseklpgPS 184
Cdd:cd07402  54 SPESY---ERLRELLAPL--PAPVYWIPGNHDD----------------RAAMREALPEPPYDDNGPVQYVV------DF 106

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104 185 RAGRVVVLNTnlyySNNEQTAGmADPGEQFRWLGDVLSNAsrDGEMVYVIGHVPP---GFfektqnkAWFRES---FNEE 258
Cdd:cd07402 107 GGWRLILLDT----SVPGVHHG-ELSDEQLDWLEAALAEA--PDRPTLIFLHHPPfplGI-------PWMDAIrlrNSQA 172

                       250       260
                ....*....|....*....|....*...
gi 19527104 259 YLKVIQKHHRVIAgQFFGHHHTDSFRMF 286
Cdd:cd07402 173 LFAVLARHPQVKA-ILCGHIHRPISGSF 199
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 22-137 4.89e-03

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 38.02  E-value: 4.89e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  22 RFWHISDLHLDPNYtvsKDPLQvcpsagsqpvlnagpwgdylcdspwaLINSSLYAMKEI-----EPKPDFILWTGD--D 94
Cdd:cd00840   1 RFLHTADWHLGYPL---YGLSR--------------------------REEDFFKAFEEIvdlaiEEKVDFVLIAGDlfD 51

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19527104  95 TPHVPNESLGEAavLAIVERLTNlikevfPDTKVYAALGNHDF 137
Cdd:cd00840  52 SNNPSPEALKLA--IEGLRRLCE------AGIPVFVIAGNHDS 86
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
22-145 6.04e-03

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 38.36  E-value: 6.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19527104  22 RFWHISDLHLdpnytvskdplqvcpsaGSQPVLNAgpwgdylcdspwaLINSSLYAMKE-----IEPKPDFILWTGD--D 94
Cdd:COG0420   2 RFLHTADWHL-----------------GKPLHGAS-------------RREDQLAALDRlvdlaIEEKVDAVLIAGDlfD 51

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19527104  95 TPHVPNEslgeaAVLAIVERLTNLIKEvfpDTKVYAALGNHDFHPKNQFPA 145
Cdd:COG0420  52 SANPSPE-----AVRLLAEALRRLSEA---GIPVVLIAGNHDSPSRLSAGS 94
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH